ID A0A084A173_9GAMM Unreviewed; 605 AA.
AC A0A084A173;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN Name=lon_2 {ECO:0000313|EMBL:KEY59052.1};
GN ORFNames=SRDD_19990 {ECO:0000313|EMBL:KEY59052.1};
OS Serratia sp. DD3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY59052.1, ECO:0000313|Proteomes:UP000017810};
RN [1] {ECO:0000313|EMBL:KEY59052.1, ECO:0000313|Proteomes:UP000017810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD3 {ECO:0000313|EMBL:KEY59052.1,
RC ECO:0000313|Proteomes:UP000017810};
RX PubMed=25212623;
RA Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT of Daphnia magna.";
RL Genome Announc. 2:e00903-14(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01122};
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEY59052.1}.
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DR EMBL; AYKS02000053; KEY59052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084A173; -.
DR STRING; 1410619.SRDD_19990; -.
DR eggNOG; COG1067; Bacteria.
DR Proteomes; UP000017810; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR041699; AAA_32.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF49; LON PROTEASE HOMOLOG-RELATED; 1.
DR Pfam; PF13654; AAA_32; 1.
DR Pfam; PF05362; Lon_C; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000313|EMBL:KEY59052.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000017810};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT DOMAIN 366..563
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 458
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 501
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 605 AA; 67815 MW; 67E61E2FE0BCD555 CRC64;
MYQAVIFLYN PLFTYYLTIT SNTLTINRLE WQSLLPSAAP YQAIFDSAAQ LAPVAFAAIQ
PRLENSLALF LHPQSQPCFM LLKAQETHEH LALIAKVTKQ LQPPHMIKGS RYVIAGGKAN
IETAVNDDEP FATHGDCIFQ QWVEPEQLFG CVRIYNGEIS LQPGLIHQAN GGVLILSARA
LLAQPLMWLR LKQMIIQRQF QWFAADETRP LPIYIPPMPL ALRLIIVGDR HSLADFDDME
PELCEQAVYG EYEDDLQLTE PDDMAQWCGY INSIIADQQL PPLAADAWYP LMVQAVRYSG
DQGNLPLSPL WISQLLSEAK LYTQEQQITA NTLEVAQNAR EWRESYLAER MHDDIELGQI
IIDTEGEVIG QINGLSVLDY PGHPRSMGEP SRISCVVHLG DGEFTDVERK AELGGNLHAK
GMMIMQAFLV SELALDQPLP FSASIVFEQS YGEVDGDSAS LAELCALISA LSQQPLTQQI
AVTGSVDQFG NVQPIGGINE KIEGFFEVCL RRGLTGQQGV ILPICNVRHL CLRADVIEAV
RNEQFHLWAV DNAGQALHLL TGYPYSDEQQ PSLLAAIQER IAQVNSHERR QWPWPLRWLN
WFNHG
//
